[Proteolytic potential of fibronectin and degradation of extracellular matrix].
Fibronectin is one of the major adhesive glycoproteins and bears interaction sites for both cell receptors and the extracellular matrix. Disappearance of fibronectin is the first step of cellular transformation in carcinogenesis. This phenomenon has been ascribed to increased proteolysis of fibronectin or of its cellular receptor. Results obtained during previous studies by the authors have shown that the fibronectin molecule has latent proteolytic activities which become apparent only after the action of other external proteases. Two proteinases, FN-gelatinase and FN-laminase, were identified in cathepsin D fibronectin digest. The acute activity of these two proteases is responsible for degradation of the extracellular matrix. Furthermore, the sequences and functions of both enzymes share a number of features with retroviral proteases.
Keil-Dlouha
V
V
Laboratoire de Chimie des Protéines, Institut Pasteur, Paris, France.
Planchenault
T
T
Imhoff
J M
JM
Emod
I
I
Blondeau
X
X
Lambert-Vidmar
S
S
D000595:Amino Acid Sequence; D010450:Endopeptidases / Q000737:chemistry / Q000494:pharmacology*; D016326:Extracellular Matrix Proteins / Q000187:drug effects* / Q000378:metabolism; D005353:Fibronectins / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D008969:Molecular Sequence Data; D010447:Peptide Hydrolases / Q000378:metabolism*
D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D010450:Endopeptidases; D010447:Peptide Hydrolases; C064016:fibronectin laminase
Potentiel protéolytique de la fibronectine et dégradation de la matrice extracellulaire.